Under slightly acidic conditions, cytosine-rich DNA sequences can form non-canonical secondary structures called i-motifs, which occur as four stretches of cytosine repeats form hemi-protonated C·C+ base pairs. The growing interest in the i-motif structures as important components in functional DNA-based nanotechnology or as potential targets of anticancer drugs, increases the need for a deep understanding of the energetics of their structural transitions. Here, a combination of spectroscopic and calorimetric techniques is used to unravel the thermodynamics of folding of an i-motif DNA under favorable conditions. The results give new insights into the energetic aspects of i-motifs and show that thermodynamic and thermal stability are related but not identical properties of such DNA structures.
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http://dx.doi.org/10.1039/d1cp01779a | DOI Listing |
Even after folding, proteins transiently sample unfolded or partially unfolded intermediates, and these species are often at risk of irreversible alteration ( via proteolysis, aggregation, or post-translational modification). Kinetic stability, in addition to thermodynamic stability, can directly impact protein lifetime, abundance, and the formation of alternative, sometimes disruptive states. However, we have very few measurements of protein unfolding rates or how mutations alter these rates, largely due to technical challenges associated with their measurement.
View Article and Find Full Text PDFDue to the hierarchical organization of RNA structures and their pivotal roles in fulfilling RNA functions, the formation of RNA secondary structure critically influences many biological processes and has thus been a crucial research topic. This review sets out to explore the computational prediction of RNA secondary structure and its connections to RNA modifications, which have emerged as an active domain in recent years. We first examine the progression of RNA secondary structure prediction methodology, focusing on a set of representative works categorized into thermodynamic, comparative, machine learning, and hybrid approaches.
View Article and Find Full Text PDFProtein Sci
February 2025
Amherst College, Amherst, Massachusetts, USA.
Hydrogen exchange mass spectrometry (HXMS) is a powerful tool to understand protein folding pathways and energetics. However, HXMS experiments to date have used exchange conditions termed EX1 or EX2 which limit the information that can be gained compared to the more general EXX exchange regime. If EXX behavior could be understood and analyzed, a single HXMS timecourse on an intact protein could fully map its folding landscape without requiring denaturation.
View Article and Find Full Text PDFJ Food Sci
January 2025
College of Tourism and Culinary Science, Yangzhou University, Yangzhou, China.
Sweet potato-oat composite dough is a nutritious, functional dough with promising market potential. This study investigates its quality changes during freeze-thaw cycles from the perspectives of ice crystals and protein alterations to provide theoretical support for its processing and production. After freeze-thaw cycles, both the storage modulus and loss modulus of the dough decrease, resulting in increased hardness, reduced resilience and chewiness, lower sensory scores, decreased specific volume, and darker color.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Biozentrum, University of Basel, Spitalstrasse 41, CH-4056 Basel, Switzerland.
The thermodynamics of pressure-induced protein denaturation could so far not be directly compared with protein denaturation induced by temperature or chemical agents. Here, we provide a new cooperative model for pressure-induced protein denaturation that allows the quantitative comparison of all three denaturing processes based on their free energy, enthalpy, entropy, and cooperativity. As model proteins, we use apolipoprotein A-1 and lysozyme.
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